ID   CA1B_CONBR              Reviewed;          13 AA.
AC   C0HLK1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   23-FEB-2022, entry version 7.
DE   RecName: Full=Alpha-conotoxin BruIB {ECO:0000303|PubMed:25466886};
OS   Conus brunneus (Wood's brown cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=101289;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   HYDROXYLATION AT PRO-7, AMIDATION AT CYS-13, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=25466886; DOI=10.1096/fj.14-262733;
RA   Heghinian M.D., Mejia M., Adams D.J., Godenschwege T.A., Mari F.;
RT   "Inhibition of cholinergic pathways in Drosophila melanogaster by alpha-
RT   conotoxins.";
RL   FASEB J. 29:1011-1018(2015).
CC   -!- FUNCTION: Acts as an inhibitor of nicotinic acetylcholine receptors
CC       (nAChR) (PubMed:25466886). Specifically inhibits the alpha-7 nAChRs of
CC       D.melanogaster, and seems to have no inhibitory effect on vertebrate
CC       nAChR subtypes (PubMed:25466886). {ECO:0000269|PubMed:25466886}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25466886}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct (at protein level).
CC       {ECO:0000269|PubMed:25466886}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..13
FT                   /note="Alpha-conotoxin BruIB"
FT                   /evidence="ECO:0000269|PubMed:25466886"
FT                   /id="PRO_0000447213"
FT   MOD_RES         7
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:25466886"
FT   MOD_RES         13
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:25466886"
FT   DISULFID        3..9
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
FT   DISULFID        4..13
FT                   /evidence="ECO:0000250|UniProtKB:P0C1D0"
SQ   SEQUENCE   13 AA;  1543 MW;  73789AA177F5B774 CRC64;
     DYCCRRPTCI PIC